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  • 1
    Electronic Resource
    Electronic Resource
    Coagulation Protein Function V (Diminution of Antithrombin III Function by Acetaldehyde) (1998)
    Springer
    Digestive diseases and sciences 43 (1998), S. 1746-1751 
    Details
    ISSN: 1573-2568
    Keywords: ANTITHROMBIN III ; THROMBIN ; ACETALDEHYDE ; ALCOHOL ; ALCOHOLISM ; BLOOD COAGULATION
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The anticoagulant activity of antithrombin III(ATIII), as observed in a plasma-free system consistingof thrombin and fibrinogen, is readily reduced byacetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM. Whereas controlthrombin-fibrinogen mixtures clotted in 17.7 ±0.75 sec, ATIII prolonged clotting time to 55.0 ±1.75 sec on preincubation with thrombin for 30 min atroom temperature. On subsequent preincubation of ATIII with theAcH for 30 min at room temperature and passage of themixture through Sephadex G-25 minicolumns to removeexcess AcH, the eluates were tested for anticoagulant activity. Clotting times of 20.9 ± 1.0,32.3 ± 1.0, and 45.3 ± 1.6 sec wereobtained with 447, 89.4, and 17.9 mM AcH-ATIII mixtures,respectively. These data suggest that functional groupson ATIII, such as guanidiniums, aminos, and others aresusceptible to adduct formation with AcH, therebyaltering the shape and charge of the anticoagulant. Asa consequence of this type of reaction, an alteredmolecule of reduced biological activity may be produced.These experimental results may explain, in part, thereduction in ATIII levels reported by others in patientswith alcoholic liver disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018831619359
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  • 2
    Electronic Resource
    Electronic Resource
    Coagulation Protein Function VI (Augmentation of Anticoagulant Function by Acetaldehyde-Treated Heparin) (1999)
    Springer
    Digestive diseases and sciences 44 (1999), S. 1349-1355 
    Details
    ISSN: 1573-2568
    Keywords: ANTITHROMBIN III ; THROMBIN ; HEPARIN ; BLOOD COAGULATION ; ACETALDEHYDE ; ALCOHOL ; ALCOHOLISM
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Acetaldehyde (AcH) at preincubationconcentrations of 447, 89.4, and 17.9 mM potentiates theeffects of heparin on the clotting time of plasma. Whilecontrol plasma clotted in the range of 12.6 ± 0.1 to 13.8 ± 0.1 sec, and heparin-treatedplasma clotted in a range from 131.5 ± 2.5 to168.2 ± 1.2 sec, heparin that was preincubated atroom temperature for 30 min with 89.4 or 447 mM AcH didnot clot plasma in 300 sec. Heparin exposed to 17.9 mMAcH clotted plasma in 193 ± 1.1 sec. Ethanol ata 404 mM concentration also prolonged the clotting timeof heparin-treated plasma 〉300 sec, while 202 mM ethanol prolonged the clotting time ofheparin-treated plasma from 149.0 ± 2.0 sec to219.5 ± 1.7 sec. It is suggested that AcH altersthe tertiary structure of heparin by adduct formation,possibly by formation of cyclic acetals with iduronicand glucuronic acids, thereby more readily affectingbinding of the glycosaminoglycan to antithrombin IIIand/or thrombin, prolonging clotting time. Ethanol, which does not react covalently with heparin,might affect its conformation as a consequence of anorganic solvent effect. Protamine sulfate prolonged theclotting time of plasma from 13.6 ± 0.1 sec to 17.9 ± 0.2 sec. Protaminesulfate-treated heparin clotted plasma in 21.0 ±0.4 sec relative to heparin-treated plasma (160.4± 1.7 sec). In subsequent experiments,AcH-treated protamine sulfate extended the clotting time of protamine sulfate from17.9 ± 0 sec to 33.7 ± 0.6 sec. Prioraddition of protamine sulfate to AcH- heparin mixturesor heparin to protamine sulfate-AcH mixtures beforeaddition to plasma resulted in clotting times of 22.0± 0.4 sec and 24.1 ± 0.5 sec,respectively, relative to control clotting times of162.3 ± 2.6 sec for plasma-heparin mixtures.These results confirm both the reduction in coagulation time ofheparin-treated plasma by protamine sulfate and theprolongation of clotting time of plasma by protaminesulfate. Furthermore, and importantly, they indicatethat acetaldehyde-treated protamine sulfate is a more effectiveanticoagulant than protamine sulfate. It is suggestedthat reversible adduct formation between acetaldehyde,heparin, and protamine sulfate may occur as a meansexplaining the essentially identical coagulation time ofthese mixtures when added to plasma regardless of theorder of premixing. Ethanol (404 mM) did not influenceprotamine sulfate effects. Lastly, the potentiation of the anticoagulant function of heparin byacetaldehyde suggests that a structural modification ofthe glycosaminoglycan may occur in alcoholics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026635331519
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  • 3
    Electronic Resource
    Electronic Resource
    Coagulation Protein Function VII (Diametric Effects of Acetaldehyde on Factor VII and Factor IX Function) (1999)
    Springer
    Digestive diseases and sciences 44 (1999), S. 2564-2567 
    Details
    ISSN: 1573-2568
    Keywords: ALCOHOL ; COAGULATION ; FACTOR VII ; FACTOR IX ; ACETALDEHYDE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The first metabolite of ethanol, acetaldehyde,has the ability to form adducts with proteins and altertheir function. It has been shown that acetaldehydereacts with various proteins of the blood coagulation pathway and, subsequently, produces aprolongation of the clotting time. This study evaluatedthe function of clotting proteins from the extrinsiccoagulation pathway (factor VII) and the intrinsiccoagulation pathway (factor IX) when preincubated withacetaldehyde as compared to a control and compared topreincubation with ethanol. Prior to use in a clottingassay, incubation times with acetaldehyde, ethanol, and the control were the same for both factorsVII and IX. An automatic fibrometer measured theclotting times. Factor VII preincubated withacetaldehyde prolonged the clotting time. However,factor IX preincubated with acetaldehyde actuallydecreased the clotting time. Of interest, both factorsVII and IX preincubated with acetaldehyde producedstatistically significant results when compared to thecontrol and ethanol. This experiment indicates thatacetaldehyde, in forming an adduct with proteins of theblood coagulation pathway, may induce a conformationalchange of factors VII and IX so as to either increase or decrease the clotting time. Therefore, it ispossible that some of the deranged coagulation inalcohol abusers may be a final net result of theinteraction of acetaldehyde and proteins of thecoagulation pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026615928562
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of the morphology and function of primary cilia in connective tissues:A cellular cybernetic probe? (1985)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 5 (1985), S. 175-193 
    Details
    ISSN: 0886-1544
    Keywords: primary cilia ; connective tissues ; secretory organelles ; extracellular matrix ; cybernetic probe ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: More than 300 primary cilia have been identified electronmicroscopically in a variety of embryonic and mature connective tissue cells. To further define the enigmatic function of these cilia, we examined the interrelationships between the basal apparatus and cytoplasmic organelles and the ciliary shaft and the extracellular matrix. The basal diplosome was consistently associated with the secretory organelles including the maturing face of the Golgi complex, Golgi vacuoles and vesicles, the microtubular network, the plasma membrane, and coated pits and vesicles. Small vesicles and amorphous granules were also observed within the ciliary lumen and adjacent to the ciliary membrane. Microtubule-membrane bridges linked axonemal tubules to the ciliary membrane. The position, projection, and orientation of the axoneme were influenced by the structural organisation and mechanical properties of the matrix and frequently caused angulation of the ciliary shaft relative to the basal body. Located midway between the secretory apparatus and the extracellular matrix, primary cilia would appear ideally situated to mediate the necessry interaction between the cell and its surrounding environment prerequisite to the formation and maintenance of a functionally effective matrix. We propose that primary cilia in connective tissue cells could act as multifunctional, cellular cybernetic probes, receiving, transducing, and conducting a variety of extrinsic stimuli to the intracellular organelles responsible for effecting the appropriate homeostatic feedback response to changes in the extracellular microenvironment.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970050302
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  • 5
    Electronic Resource
    Electronic Resource
    Second messenger function of phosphatidic acid in platelet activation (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 139 (1989), S. 558-564 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Phosphatidic acid (PA) is synthesized as the result of the receptor-mediated response of platelets to physiologic agonists. The role of PA in platelet signal transduction, however, is largely unknown. We have examined the responses of platelets to 1-stearoyl-2-arachidonoyl phosphatidic acid (SAPA), the predominant molecular species of human platelet PA. SAPA alone causes platelet aggregation, and pretreatment of platelets with SAPA markedly enhances thrombin-induced aggregation and secretion. Addition of SAPA to intact human platelets causes rapid breakdown of phosphatidylinositol-4,5-bisphosphate (PIP2) and the generation of diacylglycerol and endogenous PA. These reactions are associated with mobilization of intracellular calcium and activation of protein kinase C. SAPA also stimulates the release of endogenous arachidonic acid and its conversion to thromboxane A2. Furthermore, platelet activation by SAPA is blocked by indomethacin, indicating that the actions of SAPA are mediated by cyclooxygenase products. These findings suggest that SAPA may play an important role as an endogenous positive feedback signal to amplify receptor-mediated activation of PIP2-specific phospholipase C in human platelets.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041390315
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  • 6
    Electronic Resource
    Electronic Resource
    Increasing and decreasing protein stability: Effects of revertant substitutions on the thermal denaturation of phage λ repressor (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 217-224 
    Details
    ISSN: 0730-2312
    Keywords: mutant repressors ; differential scanning calorimetry ; protein stability ; thermal denaturation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The thermal denaturations of five revertant λ repressors containing single amino acid substitutions in their N-terminal domains have been studied by differential scanning calorimetry. Two substitutions slightly decrease stability, and the remaining three render the protein more stable than wild type. The Gly48 → Asn and Gly48 → Ser proteins are 4°C more stable than wild type. These two substitutions replace an α helical residue, and in each case a poor helix forming residue, glycine, is replaced by a residue with a higher helical propensity. We also present data showing that one revertant, Tyr22 → Phe, has reduced operator DNA binding affinity despite its enhanced stability.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240290306
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  • 7
    Electronic Resource
    Electronic Resource
    The sertoli cell junctional specializations and their relationship to the germinal epithelium as observed after efferent ductule ligation (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 183 (1975), S. 267-291 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Seminiferous tubules from testes of normal and efferent ductule ligated mice were examined with the electron microscope. The tubules in the ligated animals were markedly distended and at most stages of the seminiferous cycle the epithelium exhibited a series of circumferentially-oriented ridges. Cross-sectional profiles of these ridges were studied with particular emphasis on the Sertoli cell junctional specializations and their relationship to the germinal cells.In the ligated specimen the basal cytoplasm of the Sertoli cells is highly attenuated, often appearing as a thin process resting on the basement lamina. Where the cytoplasm of one Sertoli cell ends, it meets in apposition with the cytoplasm of an adjoining Sertoli cell, and at these sites, junctional specializations are present. The ridges are comprised of a stalk of apical Sertoli cell cytoplasm, often appearing like an inverted cone, with young spermatids aligned along the lateral surfaces and the more mature spermatid population embedded within the apical cytoplasm. Junctional specializations were observed along these lateral Sertoli cell surfaces. In some instances, they formed a free surface, but usually early spermatids were in contact with the junctional specializations. With respect to the more mature spermatids, the acrosomal component was typically found in relation to a junctional specialization. Germ cells at the spermatocyte stage were also noted in relation to the Sertoli cell junctional specializations.The findings suggest that spermatocytes cross the Sertoli cell barrier and gain access to the adluminal compartment of the seminiferous tubule through the disengagement of the inter-Sertoli cell junctional complex. It is proposed that when the inter-Sertoli cell junctional specializations separate, the spermatocytes come in apposition with the newly freed junctional surfaces and remain in relation with them through the ensuing divisions. It appears that at some point, firm adhesion between germ cells and the junctional specializations occurs; the spermatid progeny may thus maintain contact with the original inter-Sertoli cell junctional specializations until their release into the tubule lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091830205
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  • 8
    Electronic Resource
    Electronic Resource
    The Sertoli cell junctional specialization during spermiogenesis and at spermiation (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 186 (1976), S. 79-103 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The relationship between developing spermatids and Sertoli cell junctional specializations was studied with the electron microscope during spermiogenesis and at spermiation. At stage I of the seminiferous cycle, the newly formed spermatids are found in apposition to junctional specializations at the lateral surfaces of the Sertoli cell. Visualization of the junctional site of this early stage appears to be dependent on orientation and plane of section. As differentiation proceeds, the spermatids elongate and come to lie within deep recesses of the Sertoli cell. At this time the junctional specialization is limited to the acrosomal portion of the spermatid. During the maturation phase, the spermatids, while maintaining the same relationship to the junctional specialization, approach the lumen. When stage VIII of the cycle is reached, the stage in which spermiation occurs, the spermatids are at the luminal surface. The relationship of the spermatid head to the junctional specializations is quite variable during this stage. Some spermatids are observed still attached to the Sertoli cell at the junctional site, while others are found completely or partially surrounded by Sertoli cytoplasm, but with no evidence of the normally interposed junctional specialization. Yet, in other instances, the spermatids are observed in a position slightly removed from the junctional site. Also evident are profiles of junctional specializations at a free surface of the Sertoli cell, there being no attached spermatid. In some instances the junctional specializations appeared in apposition to a residual body. In the case of the free surface profiles, the junctional specialization at times lined an empty cleft or crypt-like recess, giving the impression that the spermatid head had just been dislodged from the junctional contact site. The findings indicate that the spermatid is in contact with a junctional specialization from its initial appearance and remains so until spermiation is initiated. It is postulated that spermiation is initiated through a physiological change in the junctional specialization resulting in loss of adhesion and consequent release of the sperm head from its attachment site. A similar mechanism is proposed in relation to the inter-Sertoli junctional complex to account for the means by which the spermatocytes cross this barrier to reach the adluminal compartment of the seminiferous epithelium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091860107
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  • 9
    Electronic Resource
    Electronic Resource
    Phosphorylation of the carboxy-terminal repeat domain in RNA polymerase II by cyclin-dependent kinases is sufficient to inhibit transcription (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 64 (1997), S. 390-402 
    Details
    ISSN: 0730-2312
    Keywords: carboxy-terminal repeat domain (CTD) ; RNA polymerase II ; cyclin-dependent kinases ; phosphorylation ; transcription ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Cdc2 kinase triggers the entry of mammalian cells into mitosis, the only cell cycle phase in which transcription is globally repressed. We show here that Cdc2 kinase phosphorylates components of the RNA polymerase II transcription machinery including the RNA polymerase II carboxy-terminal repeat domain (CTD). To test specifically the effect of CTD phosphorylation by Cdc2 kinase, we used a yeast in vitro transcription extract that is dependent on exogenous RNA polymerase II that contains a CTD. Phosphorylation was carried out using immobilized Cdc2 so that the kinase could be removed from the phosphorylated polymerase. ATPγS and Cdc2 kinase were used to produce an RNA polymerase 110 that was not detectably dephosphorylated in the transcription extract. RNA polymerase 110 produced in this way was defective in promoter-dependent transcription, suggesting that phosphorylation of the CTD by Cdc2 kinase can mediate transcription repression during mitosis. In addition, we show that phosphorylation of pol II with the human TFIIH-associated kinase Cdk7 also decreases transcription activity despite a different pattern of CTD phosphorylation by this kinase. These results extend previous findings that RNA polymerase 110 is defective in preinitiation complex formation. Here we demonstrate that phosphorylation of the CTD by cyclin-dependent kinases with different phosphoryl acceptor specificities can inhibit transcription in a CTD-dependent transcription system. J. Cell. Biochem. 64:390-402. © 1997 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    The organization of the seminiferous epithelium in the mouse testis following ligation of the efferent ductules. A light microscopic study (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 180 (1974), S. 565-579 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Seminiferous tubules from mouse testes were studied with the light microscope after the efferent ductules had been ligated for 48 hours. As a consequence of ligation, the tubules became markedly distended by the fluid which they accumulated; the epithelium was reduced in height, and exhibited a significantly less complex stratification than in the normal. Longitudinal sections of the distended tubules, particularly those in the early stages of the seminiferous cycle, revealed pillar-like epithelial profiles arranged in a repetitive series. Each “pillar” consisted of Sertoli cell cytoplasm along with two generations of spermatids, the older generation embedded within the Sertoli cell, and the younger generation aligned, one cell above the other, along its sides. Oblique or grazing sections through tubules exhibiting the same stages of spermiogenesis revealed band-like epithelial profiles arranged in parallel array. The two types of epithelial configurations are interpreted as representing a series of circumferentially oriented ridges within the tubule. It is postulated that each spermatid generation within a ridge constitutes a single clone, and that it is the cytoplasmic bridges joining the spermatids, in combination with their attachment to the Sertoli cells, which provide the organization, delineation, and structural stability of the ridges.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091800403
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